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Conserved domains on  [gi|30678353|ref|NP_850491|]
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carbonic anhydrase 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03014 super family cl28979
carbonic anhydrase
1-336 0e+00

carbonic anhydrase


The actual alignment was detected with superfamily member PLN03014:

Pssm-ID: 178588 [Multi-domain]  Cd Length: 347  Bit Score: 660.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353    1 MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGT 80
Cdd:PLN03014   1 MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353   81 EAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSP 160
Cdd:PLN03014  81 EAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  161 KYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFP 240
Cdd:PLN03014 161 KYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  241 LDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGA 320
Cdd:PLN03014 241 LDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGA 320
                        330
                 ....*....|....*.
gi 30678353  321 FELWGLEFGLSETSSV 336
Cdd:PLN03014 321 FELWGLEFGLSETSSV 336
 
Name Accession Description Interval E-value
PLN03014 PLN03014
carbonic anhydrase
1-336 0e+00

carbonic anhydrase


Pssm-ID: 178588 [Multi-domain]  Cd Length: 347  Bit Score: 660.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353    1 MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGT 80
Cdd:PLN03014   1 MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353   81 EAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSP 160
Cdd:PLN03014  81 EAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  161 KYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFP 240
Cdd:PLN03014 161 KYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  241 LDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGA 320
Cdd:PLN03014 241 LDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGA 320
                        330
                 ....*....|....*.
gi 30678353  321 FELWGLEFGLSETSSV 336
Cdd:PLN03014 321 FELWGLEFGLSETSSV 336
beta_CA_cladeB cd00884
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
135-324 1.56e-105

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238449  Cd Length: 190  Bit Score: 306.78  E-value: 1.56e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 135 GFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDK-VKYGGVGAAIEYA 213
Cdd:cd00884   1 GFRRFRKEYFPEERELFEKLAKGQSPKALFIACSDSRVVPALITQTQPGELFVVRNVGNLVPPYEPdGGFHGTSAAIEYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 214 VLHLKVENIVVIGHSACGGIKGLMSFPlDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLL 293
Cdd:cd00884  81 VAVLKVEHIVVCGHSDCGGIRALLSPE-DLLDKLPFIGKWLRIAEPAKEVVLAELSHADFDDQLRALEKENVLLSLENLL 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 30678353 294 TYPFVREGLVKGTLALKGGYYDFVKGAFELW 324
Cdd:cd00884 160 TYPFVRERLEAGTLSLHGWYYDIETGELYAY 190
CynT COG0288
Carbonic anhydrase [Inorganic ion transport and metabolism];
130-316 1.14e-69

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 440057  Cd Length: 204  Bit Score: 215.80  E-value: 1.14e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 130 ETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDkvkyGGVGAA 209
Cdd:COG0288   5 KRLLEGNRRFVAGKFPQDPERFEELAKGQHPFALVIGCSDSRVPPELIFDQGPGDLFVVRNAGNVVPPYD----PGVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 210 IEYAVLHLKVENIVVIGHSACGGIKGLMSfpLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSL 289
Cdd:COG0288  81 IEYAVEVLGVKLIVVLGHSGCGAVKAALD--GLELEELGLIGNWLRHIRPAVERVRAELPAADGEERLDRLVELNVREQV 158
                       170       180
                ....*....|....*....|....*..
gi 30678353 290 ANLLTYPFVREGLVKGTLALKGGYYDF 316
Cdd:COG0288 159 ENLRTSPIVREAVAAGKLKVHGWVYDL 185
Pro_CA pfam00484
Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of ...
162-319 3.70e-62

Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of non-functional homologs related to YbcF.


Pssm-ID: 459828  Cd Length: 156  Bit Score: 195.04  E-value: 3.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353   162 YMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDkvkyGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSfPL 241
Cdd:pfam00484   1 ALIIGCSDSRVPPELIFDTGPGDLFVVRNAGNLVPPYD----LNVLASIEYAVEVLKVKHIVVCGHSGCGAVKAALD-AA 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30678353   242 DGNNSTDFIEDWVKICLPAKSKVISELGDS-AFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKG 319
Cdd:pfam00484  76 GPAELPGFIDNWLRHIRPAVERVAEELESLdDPEERDDALEELNVREQVENLRTFPIVREAVAKGKLKIHGWVYDLETG 154
Pro_CA smart00947
Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the ...
155-324 5.48e-59

Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of cellular bicarbonate. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation. Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's.


Pssm-ID: 214929 [Multi-domain]  Cd Length: 154  Bit Score: 186.94  E-value: 5.48e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353    155 AKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDkvkyGGVGAAIEYAVLHLKVENIVVIGHSACGGIK 234
Cdd:smart00947   1 AKGQHPKALIIGCSDSRVPPELIFGLGPGDLFVIRNAGNIVPPYD----DGVLASLEYAVEVLGVKEIVVCGHTDCGAVK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353    235 GLMsfpldgNNSTDFIEDWVKICLPAKSKVISELGDSAfedqcgRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYY 314
Cdd:smart00947  77 AAL------DDEPGLIDNWLERIRPARERALEELGDVD------ALEELNVRDQVENLRTSPAIREAVAKGKLKVHGWVY 144
                          170
                   ....*....|
gi 30678353    315 DFVKGAFELW 324
Cdd:smart00947 145 DIETGKLEVL 154
 
Name Accession Description Interval E-value
PLN03014 PLN03014
carbonic anhydrase
1-336 0e+00

carbonic anhydrase


Pssm-ID: 178588 [Multi-domain]  Cd Length: 347  Bit Score: 660.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353    1 MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGT 80
Cdd:PLN03014   1 MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353   81 EAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSP 160
Cdd:PLN03014  81 EAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  161 KYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFP 240
Cdd:PLN03014 161 KYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  241 LDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGA 320
Cdd:PLN03014 241 LDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGA 320
                        330
                 ....*....|....*.
gi 30678353  321 FELWGLEFGLSETSSV 336
Cdd:PLN03014 321 FELWGLEFGLSETSSV 336
PLN03019 PLN03019
carbonic anhydrase
78-336 5.28e-153

carbonic anhydrase


Pssm-ID: 166660  Cd Length: 330  Bit Score: 432.65  E-value: 5.28e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353   78 MGTEAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKG 157
Cdd:PLN03019  73 MGNESYEDAIEALKKLLIEKDDLKDVAAAKVKKITAELQAASSSDSKSFDPVERIKEGFVTFKKEKYETNPALYGELAKG 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  158 QSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLM 237
Cdd:PLN03019 153 QSPKYMVFACSDSRVCPSHVLDFHPGDAFVVRNIANMVPPFDKVKYAGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLM 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  238 SFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEReAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFV 317
Cdd:PLN03019 233 SFPLDGNNSTDFIEDWVKICLPAKSKVLAESESSAFEDQCGRCER-AVNVSLANLLTYPFVREGVVKGTLALKGGYYDFV 311
                        250
                 ....*....|....*....
gi 30678353  318 KGAFELWGLEFGLSETSSV 336
Cdd:PLN03019 312 NGSFELWELQFGISPVHSI 330
PLN00416 PLN00416
carbonate dehydratase
78-328 5.06e-131

carbonate dehydratase


Pssm-ID: 177809  Cd Length: 258  Bit Score: 373.99  E-value: 5.06e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353   78 MGTEAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQtgtSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKG 157
Cdd:PLN00416   1 MATESYEAAIKGLNDLLSTKADLGNVAAAKIKALTAELK---ELDSSNSDAIERIKTGFTQFKTEKYLKNSTLFNHLAKT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  158 QSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLM 237
Cdd:PLN00416  78 QTPKFLVFACSDSRVCPSHILNFQPGEAFVVRNIANMVPPFDQKRHSGVGAAVEYAVVHLKVENILVIGHSCCGGIKGLM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  238 SFPLD-GNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDF 316
Cdd:PLN00416 158 SIEDDaAPTQSDFIENWVKIGASARNKIKEEHKDLSYDDQCNKCEKEAVNVSLGNLLSYPFVRAEVVKNTLAIRGGHYNF 237
                        250
                 ....*....|..
gi 30678353  317 VKGAFELWGLEF 328
Cdd:PLN00416 238 VKGTFDLWELDF 249
beta_CA_cladeB cd00884
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
135-324 1.56e-105

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238449  Cd Length: 190  Bit Score: 306.78  E-value: 1.56e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 135 GFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDK-VKYGGVGAAIEYA 213
Cdd:cd00884   1 GFRRFRKEYFPEERELFEKLAKGQSPKALFIACSDSRVVPALITQTQPGELFVVRNVGNLVPPYEPdGGFHGTSAAIEYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 214 VLHLKVENIVVIGHSACGGIKGLMSFPlDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLL 293
Cdd:cd00884  81 VAVLKVEHIVVCGHSDCGGIRALLSPE-DLLDKLPFIGKWLRIAEPAKEVVLAELSHADFDDQLRALEKENVLLSLENLL 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 30678353 294 TYPFVREGLVKGTLALKGGYYDFVKGAFELW 324
Cdd:cd00884 160 TYPFVRERLEAGTLSLHGWYYDIETGELYAY 190
CynT COG0288
Carbonic anhydrase [Inorganic ion transport and metabolism];
130-316 1.14e-69

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 440057  Cd Length: 204  Bit Score: 215.80  E-value: 1.14e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 130 ETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDkvkyGGVGAA 209
Cdd:COG0288   5 KRLLEGNRRFVAGKFPQDPERFEELAKGQHPFALVIGCSDSRVPPELIFDQGPGDLFVVRNAGNVVPPYD----PGVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 210 IEYAVLHLKVENIVVIGHSACGGIKGLMSfpLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSL 289
Cdd:COG0288  81 IEYAVEVLGVKLIVVLGHSGCGAVKAALD--GLELEELGLIGNWLRHIRPAVERVRAELPAADGEERLDRLVELNVREQV 158
                       170       180
                ....*....|....*....|....*..
gi 30678353 290 ANLLTYPFVREGLVKGTLALKGGYYDF 316
Cdd:COG0288 159 ENLRTSPIVREAVAAGKLKVHGWVYDL 185
PLN03006 PLN03006
carbonate dehydratase
100-331 3.52e-62

carbonate dehydratase


Pssm-ID: 178583  Cd Length: 301  Bit Score: 200.35  E-value: 3.52e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  100 LKTVAAAKVEQITAAlQTGTSSDKKA-FDPVETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVL 178
Cdd:PLN03006  53 LQVMASGKTPGLTQE-ANGVAIDRQNnTDVFDDMKQRFLAFKKLKYMDDFEHYKNLADAQAPKFLVIACADSRVCPSAVL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  179 DFQPGDAFVVRNIANMVPPFDKVKyGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGnNSTDFIEDWVKICL 258
Cdd:PLN03006 132 GFQPGDAFTVRNIANLVPPYESGP-TETKAALEFSVNTLNVENILVIGHSRCGGIQALMKMEDEG-DSRSFIHNWVVVGK 209
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30678353  259 PAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGAFELWGLEFGLS 331
Cdd:PLN03006 210 KAKESTKAVASNLHFDHQCQHCEKASINHSLERLLGYPWIEEKVRQGSLSLHGGYYNFVDCTFEKWTVDYAAS 282
Pro_CA pfam00484
Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of ...
162-319 3.70e-62

Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of non-functional homologs related to YbcF.


Pssm-ID: 459828  Cd Length: 156  Bit Score: 195.04  E-value: 3.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353   162 YMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDkvkyGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSfPL 241
Cdd:pfam00484   1 ALIIGCSDSRVPPELIFDTGPGDLFVVRNAGNLVPPYD----LNVLASIEYAVEVLKVKHIVVCGHSGCGAVKAALD-AA 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30678353   242 DGNNSTDFIEDWVKICLPAKSKVISELGDS-AFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKG 319
Cdd:pfam00484  76 GPAELPGFIDNWLRHIRPAVERVAEELESLdDPEERDDALEELNVREQVENLRTFPIVREAVAKGKLKIHGWVYDLETG 154
Pro_CA smart00947
Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the ...
155-324 5.48e-59

Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of cellular bicarbonate. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation. Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's.


Pssm-ID: 214929 [Multi-domain]  Cd Length: 154  Bit Score: 186.94  E-value: 5.48e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353    155 AKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDkvkyGGVGAAIEYAVLHLKVENIVVIGHSACGGIK 234
Cdd:smart00947   1 AKGQHPKALIIGCSDSRVPPELIFGLGPGDLFVIRNAGNIVPPYD----DGVLASLEYAVEVLGVKEIVVCGHTDCGAVK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353    235 GLMsfpldgNNSTDFIEDWVKICLPAKSKVISELGDSAfedqcgRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYY 314
Cdd:smart00947  77 AAL------DDEPGLIDNWLERIRPARERALEELGDVD------ALEELNVRDQVENLRTSPAIREAVAKGKLKVHGWVY 144
                          170
                   ....*....|
gi 30678353    315 DFVKGAFELW 324
Cdd:smart00947 145 DIETGKLEVL 154
PLN02154 PLN02154
carbonic anhydrase
124-326 2.10e-50

carbonic anhydrase


Pssm-ID: 215111  Cd Length: 290  Bit Score: 169.54  E-value: 2.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  124 KAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPfdkVKY 203
Cdd:PLN02154  71 TSYDFLDEMRHRFLKFKRQKYLPEIEKFKALAIAQSPKVMVIGCADSRVCPSYVLGFQPGEAFTIRNVANLVTP---VQN 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  204 G--GVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCE 281
Cdd:PLN02154 148 GptETNSALEFAVTTLQVENIIVMGHSNCGGIAALMSHQNHQGQHSSLVERWVMNGKAAKLRTQLASSHLSFDEQCRNCE 227
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 30678353  282 REAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGAFELWGL 326
Cdd:PLN02154 228 KESIKDSVMNLITYSWIRDRVKRGEVKIHGCYYNLSDCSLEKWRL 272
beta_CA cd00382
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
158-324 1.81e-47

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238224 [Multi-domain]  Cd Length: 119  Bit Score: 156.12  E-value: 1.81e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 158 QSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDkvkyGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGlm 237
Cdd:cd00382   1 QKPKALIIGCSDSRVPPELIFGLGPGDLFVVRNAGNLVPPYD----LDVLASLEYAVEVLGVKHIIVCGHTDCGAVKA-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 238 sfpldgnnstdfiedwvkiclpakskviselgdsafedqcgrCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFV 317
Cdd:cd00382  75 ------------------------------------------LVEENVREQVENLRSHPLIQEAVAPGELKVHGWVYDIE 112

                ....*..
gi 30678353 318 KGAFELW 324
Cdd:cd00382 113 TGKLEVL 119
beta_CA_cladeA cd00883
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
138-234 4.70e-34

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238448  Cd Length: 182  Bit Score: 123.44  E-value: 4.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 138 KFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKvkygGVGAAIEYAVLHL 217
Cdd:cd00883   3 AWAEEKKAKDPDFFPRLAKGQTPEYLWIGCSDSRVPENTILGLLPGEVFVHRNIANLVSPTDL----NCLSVLQYAVDVL 78
                        90
                ....*....|....*..
gi 30678353 218 KVENIVVIGHSACGGIK 234
Cdd:cd00883  79 KVKHIIVCGHYGCGGVK 95
beta_CA_cladeC cd03378
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
130-235 7.13e-23

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 239473 [Multi-domain]  Cd Length: 154  Bit Score: 92.97  E-value: 7.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353 130 ETIKQG---FIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPfdkvkygGV 206
Cdd:cd03378   6 ERLKEGnkrFVSGKPLHPDQDLARRRELAKGQKPFAVILSCSDSRVPPEIIFDQGLGDLFVVRVAGNIVDD-------DV 78
                        90       100
                ....*....|....*....|....*....
gi 30678353 207 GAAIEYAVLHLKVENIVVIGHSACGGIKG 235
Cdd:cd03378  79 LGSLEYAVEVLGVPLVVVLGHESCGAVAA 107
PRK10437 PRK10437
carbonic anhydrase; Provisional
145-255 2.03e-17

carbonic anhydrase; Provisional


Pssm-ID: 182460  Cd Length: 220  Bit Score: 79.59  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  145 ETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKvkygGVGAAIEYAVLHLKVENIVV 224
Cdd:PRK10437  20 EEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDL----NCLSVVQYAVDVLEVEHIII 95
                         90       100       110
                 ....*....|....*....|....*....|....
gi 30678353  225 IGHSACGGIKGLMSFPLDG--NNSTDFIED-WVK 255
Cdd:PRK10437  96 CGHYGCGGVQAAVENPELGliNNWLLHIRDiWFK 129
PRK15219 PRK15219
carbonic anhydrase; Provisional
103-235 2.07e-08

carbonic anhydrase; Provisional


Pssm-ID: 237927 [Multi-domain]  Cd Length: 245  Bit Score: 54.07  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678353  103 VAAAKVEQIT-AALQTGTSSDKKAFDPV-ETIKQGFIKFKkekyETNPALYGELA------KGQSPKYMVFACSDSRVCP 174
Cdd:PRK15219  29 LAGLGVPQISyAASLTKEERDKMTPDQIiESLKQGNKRFR----SGKPAQHDYLAqkrasaAGQYPAAVILSCIDSRAPA 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30678353  175 SHVLDFQPGDAF---VVRNIANmvppfdkvkyGGVGAAIEYAVLHLKVENIVVIGHSACGGIKG 235
Cdd:PRK15219 105 EIILDTGIGETFnsrVAGNISN----------DDLLGSMEFACAVAGAKVVLVMGHTACGAVKG 158
beta_CA_cladeD cd03379
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
159-231 9.89e-08

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 239474  Cd Length: 142  Bit Score: 50.33  E-value: 9.89e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30678353 159 SPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVppfdkvkyggVGAAIEYAVL---HLKVENIVVIGHSACG 231
Cdd:cd03379   2 ARKLAIVTCMDARLDPEKALGLKLGDAKVIRNAGGRV----------TDDAIRSLVVsvyLLGTREIIVIHHTDCG 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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